Information on EC 3.1.12.2 - DNA-3'-diphospho-5'-guanosine diphosphatase

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The expected taxonomic range for this enzyme is: Schizosaccharomyces pombe

EC NUMBER
COMMENTARY hide
3.1.12.2
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RECOMMENDED NAME
GeneOntology No.
DNA-3'-diphospho-5'-guanosine diphosphatase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[DNA]-3'-diphospho-5'-guanosine + H2O = [DNA]-3'-phosphate + GMP
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
[DNA]-3'-diphospho-5'-guanosine hydrolase (guanosine 5'-phosphate-forming)
Aprataxin is a DNA-binding protein that catalyses (among other activities) the 3' decapping of DNA-ppG (formed by EC 6.5.1.8, 3'-phosphate/5'-hydroxy nucleic acid ligase) [1]. The enzyme binds the guanylate group to a histidine residue at its active site, forming a covalent enzyme-nucleotide phosphate intermediate, followed by the hydrolysis of the guanylate from the nucleic acid and its eventual release. The enzyme also possesses the activity of EC 3.1.11.7, adenosine-5'-diphospho-5'-[DNA] diphosphatase, and EC 3.1.11.8, guanosine-5'-diphospho-5'-[DNA] diphosphatase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
[DNA]-3'-diphospho-5'-(6-O-methylguanosine) + H2O
[DNA]-3'-phosphate + 6-O-methyl-GMP
show the reaction diagram
[DNA]-3'-diphospho-5'-guanosine + H2O
[DNA]-3'-phosphate + GMP
show the reaction diagram
[DNA]-3'-diphospho-5'-inosine + H2O
[DNA]-3'-phosphate + IMP
show the reaction diagram
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additional information
?
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure in complex with GMP, to 1.5 A resolution. GMP binds at the same position and in the same anti nucleoside conformation as AMP, and aprataxin makes more extensive nucleobase contacts with guanine than with adenine, via a hydrogen bonding network to the guanine O6, N1, N2 base edge
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D63A
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mutation impairs DNAppG decapping
His147A
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mutation abolishes DNAppG decapping activity
His149A
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mutation abolishes DNAppG decapping activity
D63A
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mutation impairs DNAppG decapping
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His147A
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mutation abolishes DNAppG decapping activity
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His149A
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mutation abolishes DNAppG decapping activity
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